Conservation of a crystallographic interface suggests a role for β-sheet augmentation in influenza virus NS1 multifunctionality
Conservation of a crystallographic interface suggests a role for β-sheet augmentation in influenza virus NS1 multifunctionality
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DOI：
10.1107/s1744309111019312
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发表时间：
2011-08-01
影响因子：
0.9
通讯作者：
Russell, Rupert J. M.
中科院分区：
文献类型：
--
作者：
Kerry, Philip S.;Long, Elizabeth;Russell, Rupert J. M.
流感病毒毒力因子NS 1的效应结构域（艾德）能够与多种细胞和病毒靶标相互作用，尽管对这些事件的调控知之甚少。将W187 A突变引入艾德中消除了二聚体形成;然而，在两种先前的晶体形式中已经观察到突变NS 1艾德单体之间的链-链相互作用。使用悬滴气相扩散法发现了该蛋白质结晶的新条件[0.1 M Bis-Tris pH 6.0，0.2 M NaCl，22%（w/v）PEG 3350，20 mM木糖醇]。从在40 mM噻吩并[2，3-B]-吡啶-2-基甲醇存在下生长的晶体收集延伸至1.8埃分辨率的衍射数据。有人观察到，在三个不同的空间群中，这种单体NS 1艾德的晶体中的链-链界面是保守的。这一观察结果，加上界面区域的构象变化，表明β-折叠增强NS 1功能的潜在作用。
The effector domain (ED) of the influenza virus virulence factor NS1 is capable of interaction with a variety of cellular and viral targets, although regulation of these events is poorly understood. Introduction of a W187A mutation into the ED abolishes dimer formation; however, strand-strand interactions between mutant NS1 ED monomers have been observed in two previous crystal forms. A new condition for crystallization of this protein [0.1 M Bis-Tris pH 6.0, 0.2 M NaCl, 22%(w/v) PEG 3350, 20 mM xylitol] was discovered using the hanging-drop vapour-diffusion method. Diffraction data extending to 1.8 angstrom resolution were collected from a crystal grown in the presence of 40 mM thieno[2,3-b]-pyridin-2-ylmethanol. It was observed that there is conservation of the strand-strand interface in crystals of this monomeric NS1 ED in three different space groups. This observation, coupled with conformational changes in the interface region, suggests a potential role for beta-sheet augmentation in NS1 function.